An SEM Study Of The Effect of Altering the Reaction pH on Fluoride Catalysed Silica Sol-Gel Templating Of Self-Assembling Peptide Fibrils

摘要

Biomolecules such as proteins, peptides and also other naturally occurring biomimetic or synthetic self-assembling systems (as analogues of naturally occurring species or polymers containing unnatural amino acids) can be used as organic templates for silica deposition. The use of such templates allows for synthesis of nanostructured materials over a wide pH range and through careful choice or design of the template can provide a unique way of understanding the processes involved in silica biomineralisation. Naturally occurring and synthetic peptides adopt two major types of ordered secondary structure, the a helix and the β sheet (fig. 1A, 1B). Of the two secondary structures the more stable is the βsheet, β sheets arise due to hydrogen bonding interactions between several amino acid residues on adjacent (or in some cases, the same) peptide chains. Peptide molecules have been engineered by the Aggeli group to aggregate and form tapes, ribbons and eventually twisted rope like fibrils. All the aggregated structures exhibit the chirality dictated by their constituent amino acid monomers.